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Database: UniProt
Entry: A0A172T7M2_9DEIO
LinkDB: A0A172T7M2_9DEIO
Original site: A0A172T7M2_9DEIO 
ID   A0A172T7M2_9DEIO        Unreviewed;       527 AA.
AC   A0A172T7M2;
DT   07-SEP-2016, integrated into UniProtKB/TrEMBL.
DT   07-SEP-2016, sequence version 1.
DT   27-MAR-2024, entry version 27.
DE   SubName: Full=Peptidase S8 {ECO:0000313|EMBL:ANE42980.1};
GN   ORFNames=SU48_03450 {ECO:0000313|EMBL:ANE42980.1};
OS   Deinococcus puniceus.
OC   Bacteria; Deinococcota; Deinococci; Deinococcales; Deinococcaceae;
OC   Deinococcus.
OX   NCBI_TaxID=1182568 {ECO:0000313|EMBL:ANE42980.1, ECO:0000313|Proteomes:UP000077363};
RN   [1] {ECO:0000313|EMBL:ANE42980.1, ECO:0000313|Proteomes:UP000077363}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=DY1 {ECO:0000313|EMBL:ANE42980.1,
RC   ECO:0000313|Proteomes:UP000077363};
RA   Kim M.K., Srinivasan S., Lee J.-J.;
RT   "Deinococcus puniceus/DY1/ whole genome sequencing.";
RL   Submitted (JAN-2015) to the EMBL/GenBank/DDBJ databases.
CC   -!- SIMILARITY: Belongs to the peptidase S8 family.
CC       {ECO:0000256|ARBA:ARBA00011073, ECO:0000256|PROSITE-ProRule:PRU01240,
CC       ECO:0000256|RuleBase:RU003355}.
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DR   EMBL; CP011387; ANE42980.1; -; Genomic_DNA.
DR   RefSeq; WP_064014038.1; NZ_CP011387.1.
DR   AlphaFoldDB; A0A172T7M2; -.
DR   STRING; 1182568.SU48_03450; -.
DR   KEGG; dpu:SU48_03450; -.
DR   PATRIC; fig|1182568.3.peg.722; -.
DR   OrthoDB; 9798386at2; -.
DR   Proteomes; UP000077363; Chromosome.
DR   GO; GO:0004252; F:serine-type endopeptidase activity; IEA:UniProtKB-UniRule.
DR   GO; GO:0006508; P:proteolysis; IEA:UniProtKB-KW.
DR   CDD; cd04077; Peptidases_S8_PCSK9_ProteinaseK_like; 1.
DR   Gene3D; 2.60.120.380; -; 1.
DR   Gene3D; 3.30.70.80; Peptidase S8 propeptide/proteinase inhibitor I9; 1.
DR   Gene3D; 3.40.50.200; Peptidase S8/S53 domain; 1.
DR   InterPro; IPR034193; PCSK9_ProteinaseK-like.
DR   InterPro; IPR000209; Peptidase_S8/S53_dom.
DR   InterPro; IPR036852; Peptidase_S8/S53_dom_sf.
DR   InterPro; IPR023827; Peptidase_S8_Asp-AS.
DR   InterPro; IPR022398; Peptidase_S8_His-AS.
DR   InterPro; IPR023828; Peptidase_S8_Ser-AS.
DR   InterPro; IPR015500; Peptidase_S8_subtilisin-rel.
DR   InterPro; IPR010259; S8pro/Inhibitor_I9.
DR   InterPro; IPR037045; S8pro/Inhibitor_I9_sf.
DR   PANTHER; PTHR43806:SF59; CEREVISIN-RELATED; 1.
DR   PANTHER; PTHR43806; PEPTIDASE S8; 1.
DR   Pfam; PF05922; Inhibitor_I9; 1.
DR   Pfam; PF00082; Peptidase_S8; 1.
DR   PRINTS; PR00723; SUBTILISIN.
DR   SUPFAM; SSF89260; Collagen-binding domain; 1.
DR   SUPFAM; SSF54897; Protease propeptides/inhibitors; 1.
DR   SUPFAM; SSF52743; Subtilisin-like; 1.
DR   PROSITE; PS51257; PROKAR_LIPOPROTEIN; 1.
DR   PROSITE; PS51892; SUBTILASE; 1.
DR   PROSITE; PS00136; SUBTILASE_ASP; 1.
DR   PROSITE; PS00137; SUBTILASE_HIS; 1.
DR   PROSITE; PS00138; SUBTILASE_SER; 1.
PE   3: Inferred from homology;
KW   Hydrolase {ECO:0000256|ARBA:ARBA00022801, ECO:0000256|PROSITE-
KW   ProRule:PRU01240};
KW   Protease {ECO:0000256|ARBA:ARBA00022670, ECO:0000256|PROSITE-
KW   ProRule:PRU01240}; Reference proteome {ECO:0000313|Proteomes:UP000077363};
KW   Serine protease {ECO:0000256|ARBA:ARBA00022825, ECO:0000256|PROSITE-
KW   ProRule:PRU01240}; Signal {ECO:0000256|SAM:SignalP}.
FT   SIGNAL          1..32
FT                   /evidence="ECO:0000256|SAM:SignalP"
FT   CHAIN           33..527
FT                   /evidence="ECO:0000256|SAM:SignalP"
FT                   /id="PRO_5008000456"
FT   DOMAIN          64..142
FT                   /note="Inhibitor I9"
FT                   /evidence="ECO:0000259|Pfam:PF05922"
FT   DOMAIN          174..403
FT                   /note="Peptidase S8/S53"
FT                   /evidence="ECO:0000259|Pfam:PF00082"
FT   ACT_SITE        183
FT                   /note="Charge relay system"
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU01240"
FT   ACT_SITE        215
FT                   /note="Charge relay system"
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU01240"
FT   ACT_SITE        367
FT                   /note="Charge relay system"
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU01240"
SQ   SEQUENCE   527 AA;  52795 MW;  C349C252EB6E9A79 CRC64;
     MARLTPIVSA GTLALTLLLA SCGSQPTETA LAAPDAAQAA GPDRAARIEA PLLGTANPDA
     IPGQYIVVMS EGSVSGLSAQ GLSAQNAGSL IRALSLDPQG VTVQQVYTQA IEGFAGKLSA
     QNLQTLRADP RVKYIEQDGV MRANATQTGA TWGLDRIDQR DLPLNGSYSY TPTGSGVTAY
     IIDTGINIGH TNFGGRAVWG TNTTGDGNNS DCQGHGTHVA GTVGSATWGV AKAVKLVAVK
     VLDCAGSGSN SGVIAGINWA VSNKTGPAVA NMSLGGGASQ AVDDAVNSAS SRNLVMVVAA
     GNENQNACNV SPARAASAIT VGSTTRTDAR SSFSNFGSCV DIFAPGSDIT STWIGSTTAT
     NTISGTSMAS PHVAGAVALL LQGTPSGSSS AITSSLISAS TPNKVTGAGT GSPNRLLFTG
     TGGTTPPPTG TTTTYTGSVS NRTSSYKPGT GGFSYAGGTL KGNLSAASGT DFDLFLQKYN
     GSAWADVASS EGSSSTEAIS YAAGSGTYRW EVYAYSGSGN YTLVETK
//
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